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Chapter 1
Chapter 1

... by uniport systems, whereas solute accumulation usually requires that transport is coupled to the co-transport (symport) of monovalent cations, mostly H+ or Na+. When a substrate is pumped out against its concentration gradient, energy coupling involves substrate:H+ or Na+ countertransport (antiport ...
Journal of Bacteriology
Journal of Bacteriology

... FIG. 1. nod sequences present in plasmids used in this study. (A) Part of pRLlJI is shown on the top line; open reading frames of the nod genes are represented as open boxes. Plasmid pMP2004 contains all of the nodlJ genes, and pMP2008 contains the entire nodI gene and nodJ sequences up to the BglII ...
CHAPTER 6 Gene Expression: Translation
CHAPTER 6 Gene Expression: Translation

... 台大農藝系 遺傳學 601 20000 Chapter 5 slide 10 ...
Activities for the -Helix and -Sheet Construction Kit
Activities for the -Helix and -Sheet Construction Kit

... The primary sequence of a protein, composed of amino acids, determines the organization of the sequence into the secondary structure. There are two periodic secondary structure motifs, α-helix and β-sheet. Proteins can be composed of primarily α-helices (for example, β-globin) or β-sheets (for examp ...
Combinatorial mutagenesis to restrict amino acid usage in an
Combinatorial mutagenesis to restrict amino acid usage in an

sample written evaluation
sample written evaluation

Key To Problem Set 3R
Key To Problem Set 3R

... A-2. The enzyme that releases AP from the lysosomal membrane is probably found (on the lumen side of the lysosomal membrane) AND A-3. The enzyme probably cuts (on the amino side of a stop transfer sequence) . Explanation: The protein enters the ER using its SP on the amino end. If the SP were the on ...
08A-MembraneStructure
08A-MembraneStructure

... • Cells recognize other cells by keying on surface molecules, often carbohydrates, on the plasma membrane. Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings ...
08A-MembraneStructure
08A-MembraneStructure

... • Cells recognize other cells by keying on surface molecules, often carbohydrates, on the plasma membrane. Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings ...
Protein structure and function
Protein structure and function

... Structure and function of myoglobin Myoglobin, a hemeprotein present in heart and skeletal muscle, functions both as a reservoir for oxygen, and as an oxygen carrier that increases the rate of transport of oxygen within the muscle cell. Myoglobin consists of a single polypeptide chain that is struct ...
lecturenotes.pdf
lecturenotes.pdf

... Details of Protein Folding - see additional handout Details of Protein Processing In the Golgi various sugars are added to various sites in the protein. This process is called glycosylation. Often glycosylation is necessary for a protein to be active. ...
Dark induction and subcellular localization of the pathogenesis
Dark induction and subcellular localization of the pathogenesis

... 15-fold increase of GUS activity was detected (Fig. 5C). Thus, the 863 bp PRB-lb promoter responds to ethylene induction, but not to darkness. The responsiveness to darkness of other regions of the gene was tested in four independent transgenic plants containing the PRB-lb coding region and 3 kb of ...
Translation - The Citadel
Translation - The Citadel

... the proper protein sequence of amino acids??? The genetic code = the way that the 4 bases of RNA encode the amino acid sequence of protein. Proteins are made of monomers called amino acids. There are 20 different amino acids. Each protein is made of a different combination of a.a.'s. A messenger RNA ...
Presentation - people.vcu.edu
Presentation - people.vcu.edu

... Hugenholtz, P., et al, (2000) Investigation of Candidate Division TM7, a Recently Recognized Major Lineage of the Domain Bacteria with No Known Pure-Culture Representatives. Applied and Environmental Microbiology, 67, 411-419. ...
Organic compounds
Organic compounds

The 11th lecture in molecular biology
The 11th lecture in molecular biology

... Structure of m RNA: Messenger RNA carries information from DNA to the ribosome, the sites of protein synthesis (translation) in the cell. The coding sequence of the mRNA determines the amino acid sequence in the protein . The basic differences in m RNA structure in prokaryotic and Eukaryotic mRNAs o ...
N-fluoroacetylglucosamine. This substance is known
N-fluoroacetylglucosamine. This substance is known

... biosynthesis of an oligosaccharide chain requires: (a) the attachment of a monosaccharide to a specific amino acid [serine, threonine, hydroxylysine, hydroxyproline, asparagine or cysteine; asparagine in the typical linkage region -Asn-X-Thr/Ser-, with X being any amino acid (Spiro, 1970)]; (b) the ...
Amino Acids 2 Questions
Amino Acids 2 Questions

... Amino Acid Composition of Proteins ...
BIOANALYTICAL/CLINICAL ANALYSIS
BIOANALYTICAL/CLINICAL ANALYSIS

... T3 and T4 Important-Assayed by Immunology,old method RadioImmunoassay,Now Enzyme Immunoassay with Antibodies ...
Name___________________________ Lab #______ Role: Activity
Name___________________________ Lab #______ Role: Activity

... Complete the steps of protein synthesis from Activity 1 with the altered DNA strand from Step 3. Begin with transcribing the altered DNA into mRNA. Record the mRNA strand below. (Note: Cross off any beads you do not use with an X.) ...
Proteins are made of chains of amino acids
Proteins are made of chains of amino acids

... HOW is the shape of a protein determined? WHY does heating/boiling denature enzymes and make them lose their function? Also: • What makes hair straight or curly and how do perms work? • Why is it important to eat different types of food to supply our protein needs? ...
ION BINDING TO BIO
ION BINDING TO BIO

... ions (1). Traditionally, the latter falls under the category of Hofmeister or ion-specific effects which in recent years has seen an appreciable renaissance – both from experimental and theoretical perspectives. In Hofmeister's original studies (2) ions were arranged according to their ability to pr ...
How to  build  a  glycinergic  postsynaptic ...
How to build a glycinergic postsynaptic ...

... genomic sequences encoding a fourth variant, a4, have been isolated from mouse (Y. Maulet, B. Matzenbach, and H. Betz, unpublished observations). All these a sequences display a high degree of amino acid identity and correspond to GlyR proteins, whose expression is under distinct temporal and region ...
Heat Shock Proteins
Heat Shock Proteins

... Heat Sh o ck Pro tein s BPS Bioscience offers a wide range of high purity HSPs for drug discovery research. ...
The mapping of linear B-cell epitope regions in desmoglein 1 and 3
The mapping of linear B-cell epitope regions in desmoglein 1 and 3

... similarity to the native antigen which allows the binding of antibodies. This is a rapid, practical, and cost-effective method for linear epitope region identification [20, 21]. B-cell epitope mapping using a series of pin-attached overlapping synthetic peptides can be a very efficient way to identi ...
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Protein



Proteins (/ˈproʊˌtiːnz/ or /ˈproʊti.ɨnz/) are large biomolecules, or macromolecules, consisting of one or more long chains of amino acid residues. Proteins perform a vast array of functions within living organisms, including catalyzing metabolic reactions, DNA replication, responding to stimuli, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific three-dimensional structure that determines its activity.A linear chain of amino acid residues is called a polypeptide. A protein contains at least one long polypeptide. Short polypeptides, containing less than about 20-30 residues, are rarely considered to be proteins and are commonly called peptides, or sometimes oligopeptides. The individual amino acid residues are bonded together by peptide bonds and adjacent amino acid residues. The sequence of amino acid residues in a protein is defined by the sequence of a gene, which is encoded in the genetic code. In general, the genetic code specifies 20 standard amino acids; however, in certain organisms the genetic code can include selenocysteine and—in certain archaea—pyrrolysine. Shortly after or even during synthesis, the residues in a protein are often chemically modified by posttranslational modification, which alters the physical and chemical properties, folding, stability, activity, and ultimately, the function of the proteins. Sometimes proteins have non-peptide groups attached, which can be called prosthetic groups or cofactors. Proteins can also work together to achieve a particular function, and they often associate to form stable protein complexes.Once formed, proteins only exist for a certain period of time and are then degraded and recycled by the cell's machinery through the process of protein turnover. A protein's lifespan is measured in terms of its half-life and covers a wide range. They can exist for minutes or years with an average lifespan of 1–2 days in mammalian cells. Abnormal and or misfolded proteins are degraded more rapidly either due to being targeted for destruction or due to being unstable.Like other biological macromolecules such as polysaccharides and nucleic acids, proteins are essential parts of organisms and participate in virtually every process within cells. Many proteins are enzymes that catalyze biochemical reactions and are vital to metabolism. Proteins also have structural or mechanical functions, such as actin and myosin in muscle and the proteins in the cytoskeleton, which form a system of scaffolding that maintains cell shape. Other proteins are important in cell signaling, immune responses, cell adhesion, and the cell cycle. Proteins are also necessary in animals' diets, since animals cannot synthesize all the amino acids they need and must obtain essential amino acids from food. Through the process of digestion, animals break down ingested protein into free amino acids that are then used in metabolism.Proteins may be purified from other cellular components using a variety of techniques such as ultracentrifugation, precipitation, electrophoresis, and chromatography; the advent of genetic engineering has made possible a number of methods to facilitate purification. Methods commonly used to study protein structure and function include immunohistochemistry, site-directed mutagenesis, X-ray crystallography, nuclear magnetic resonance and mass spectrometry.
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